ID A0A067EWS1_CITSI Unreviewed; 1129 AA.
AC A0A067EWS1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=CISIN_1g045995mg {ECO:0000313|EMBL:KDO58325.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO58325.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO58325.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
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DR EMBL; KK784950; KDO58325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067EWS1; -.
DR STRING; 2711.A0A067EWS1; -.
DR PaxDb; 2711-XP_006464641-1; -.
DR eggNOG; KOG0903; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..141
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 846..1114
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 127947 MW; 3E7308D21994A92D CRC64;
MVRLLGLSIR ESDESPREIT PRTHLTSESS ENGWLIRFFD SSFFCEWIAV SYLYKHDHAG
VRDYLCNRMY TLPLTGIEGY LFQICYMMIH KPSPSLDKFV IDICSKSLKI ALKVHWFLMA
ELEDSDDNEG ISRIQEKCQI AATLMGEWPP LVRVPNSGSS PGTKNQVLNK LLSSKQRLLS
LTSSPPTPRS LSFSSPSGNN LQEDANQSTL EENKIFKKFI PGPKMRDALL FRKSVEKDEE
ESEKDGFFKR LLRDSRGEDE EMTSSSEGFF KRLLRDSKGD DDELMSSSEG FFKKLFRDSK
SDFDDKSVSK SLEDDEKDGF FKKFFKEKFE DKKDGSHRNE GEEVVNIEEK CSKSTEDDEK
EGFFKKFFKE KFEDKKDGSH RNEDEEVVNT EEKCSKSTED DEKEGFFRKF FKEKFEDKKD
GNEKNDEGNS GIEEEESSDF SLFRRLFRVH PEDPKRAAAS ENSNSGGMFE SSPGTENFFR
KLFRDRDRSV EDSELFGSKK QREKRPGSPK QQNEKSNSKP PLPVNIASQF RKGAYHESLD
FVMSLCDTSY GLVDIFPVED RKPALRESLA EINLHIAESQ NMGGICFPMG KGLYRVVHIP
EDEAVLLNSR EKAPYMICVE VLKCETPSNA KDTSGPQKLS RGGIPLANGD AFLPKPPPWA
YPLWTAQEAY RNSTDRMSES TAQAIDQAMT HKSDAKVKLV NLSLSVEKHV HIQSKNPDAP
VTQSGINFSG MLPAAVHTTS NSNQIGEGVS HTSRAINDLE WVRVVLTADP GVRMEDIEYQ
GPPRRKEHRR VPSTVAIEEV KAAAAKGEAP PGLPLKGAGQ DSSDAKPRAN GGIPRATDAL
SGELWEVKKE RIRKASAYGK SPGWDLRSVI VKSGDDCRQE HLAVQLISHF YDIFQEAGLP
LWLRPYEVLV TSSYTALIET IYDTASLHSI KSRYPNITSL RDFFVAKYQE NSPSFKLAQR
NFVESMAGYS LVCYLLQVKD RHNGNLLLDE EGHIIHIDFG FMLSNSPGGV NFESAPFKLT
RELLEVMDSD AEGLPSEFFD YFKVLCIQGF LTCRKHAERI ILLVEMLQDS GFPCFKGGPR
TIQNLRKRFH LSLTEEQCVS LVLSLISSSL DAWRTRQYDY YQRVLNGIL
//
